Abstract
Background Solute carrier 6 (SLC6) membrane proteins are integral membrane proteins and of particular pharmacological interest because they are targets of many clinically important drugs. These SLC6 proteins play crucial roles ranging from nutrient uptake to neurotransmitter clearance. A leucine transporter LeuTAa from Aquifex aeolicus has been recognized as a bacterial orthologue of mammalian SLC6 family proteins. LeuTAa has been crystallized and its structure was resolved to high resolution. With respect to its kinship to other SLC6 transporters, though with low sequence identity (~20–25%), there are crucial regions in transmembrane segments 1, 3, 6 and 8 where conservation reaches ~50%. For this very reason LeuTAa provides a good structural paradigm to study homology models of SLC6 family members and learn more about the structure/function relationship in mammalian transporters.
Highlights
Solute carrier 6 (SLC6) membrane proteins are integral membrane proteins and of particular pharmacological interest because they are targets of many clinically important drugs. These SLC6 proteins play crucial roles ranging from nutrient uptake to neurotransmitter clearance
A leucine transporter LeuTAa from Aquifex aeolicus has been recognized as a bacterial orthologue of mammalian SLC6 family proteins
LeuTAa has been crystallized and its structure was resolved to high resolution
Summary
Solute carrier 6 (SLC6) membrane proteins are integral membrane proteins and of particular pharmacological interest because they are targets of many clinically important drugs These SLC6 proteins play crucial roles ranging from nutrient uptake to neurotransmitter clearance. With respect to its kinship to other SLC6 transporters, though with low sequence identity (~20–25%), there are crucial regions in transmembrane segments 1, 3, 6 and 8 where conservation reaches ~50%. For this very reason LeuTAa provides a good structural paradigm to study homology models of SLC6 family members and learn more about the structure/function relationship in mammalian transporters
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